1x9l

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Solution structure of CuI-DR1885 from Deinococcus Radiodurans

Overview

Sco1 and Cox17 are accessory proteins required for the correct assembly of, eukaryotic cytochrome c oxidase. At variance with Sco1, Cox17 orthologs, are found only in eukaryotes. We browsed bacterial genomes to search, proteins functionally equivalent to Cox17, and we identified a class of, proteins of unknown function displaying a conserved gene neighborhood to, bacterial Sco1 genes, all sharing a potential metal binding motif, H(M)X10MX21HXM. Two members of this group, DR1885 from Deinococcus, radiodurans and CC3502 from Caulobacter crescentus, were expressed, and, their interaction with copper was investigated. The solution structure and, extended x-ray absorption fine structure data on the former protein reveal, that the protein binds copper(I) through a histidine and three Mets in a, cupredoxin-like fold. The surface location of the copper-binding site as, well as the type of coordination are well poised for metal transfer, chemistry, suggesting that DR1885 might transfer copper, taking the role, of Cox17 in bacteria. On the basis of our results, a possible pathway for, copper delivery to the Cu(A) center in bacteria is proposed.

About this Structure

1X9L is a Single protein structure of sequence from Deinococcus radiodurans r1 with CU1 as ligand. Full crystallographic information is available from OCA.

Reference

A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase., Banci L, Bertini I, Ciofi-Baffoni S, Katsari E, Katsaros N, Kubicek K, Mangani S, Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3994-9. Epub 2005 Mar 7. PMID:15753304

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